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Ion binding properties in acetonitrile of cyclo‐peptides built u from proline and glycine residues

MPG-Autoren
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Wieland,  Theodor
Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://onlinelibrary.wiley.com/doi/epdf/10.1111/j.1399-3011.1977.tb02805.x
(beliebiger Volltext)

https://doi.org/10.1111/j.1399-3011.1977.tb02805.x
(beliebiger Volltext)

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Zitation

Hollosi, M., & Wieland, T. (1977). Ion binding properties in acetonitrile of cyclo‐peptides built u from proline and glycine residues. International Journal Peptide Protein Research, 10(5), 329-341. doi:10.1111/j.1399-3011.1977.tb02805.x.


Zitierlink: https://hdl.handle.net/21.11116/0000-0002-CA23-3
Zusammenfassung
Ion binding properties of antamanide‐like cyclopeptides cyclo‐(Pro2–Glyn‐Pro2–Glym) (n, m = 1–3) have been studied by CD spectroscopy and by conductivity measurements. Cyclo‐(Pro2–Gly‐Pro2–Gly) forming complexes of different stoichiometry can be characterized by a strong preference of selectivity for Mg++ and Ca++ ions over alkali ions whereas the other members of the series bind selectively alkali and alkaline earth cations with ion radius of about 1 Å. Three main types of CD spectra of cyclic peptides and their complexes can be differentiated. Type I showing two negative Cotton effects at around 220 nm and 200 nm (Ib, Fig. 3), type II showing a positive band around 220 nm and a strong negative one below 190 nm (e.g. Ic in acetonitrile, Fig. 4), and type III showing a strong negative band in the 205 nm region (e.g. metal complexes of Id, Fig. 6).